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Inhibition of curli assembly and Escherichia coli biofilm formation by the human systemic amyloid precursor transthyretin
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
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2017 (Engelska)Ingår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 114, nr 46, s. 12184-12189Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

During biofilm formation, Escherichia coli and other Enterobacteriaceae produce an extracellular matrix consisting of curli amyloid fibers and cellulose. The precursor of curli fibers is the amyloidogenic protein CsgA. The human systemic amyloid precursor protein transthyretin (TTR) is known to inhibit amyloid-β (Aβ) aggregation in vitro and suppress the Alzheimer’s-like phenotypes in a transgenic mouse model of Aβ deposition. We hypothesized that TTR might have broad antiamyloid activity because the biophysical properties of amyloids are largely conserved across species and kingdoms. Here, we report that both human WT tetrameric TTR (WT-TTR) and its engineered nontetramer-forming monomer (M-TTR, F87M/L110M) inhibit CsgA amyloid formation in vitro, with M-TTR being the more efficient inhibitor. Preincubation of WT-TTR with small molecules that occupy the T4 binding site eliminated the inhibitory capacity of the tetramer; however, they did not significantly compromise the ability of M-TTR to inhibit CsgA amyloidogenesis. TTR also inhibited amyloid-dependent biofilm formation in two different bacterial species with no apparent bactericidal or bacteriostatic effects. These discoveries suggest that TTR is an effective antibiofilm agent that could potentiate antibiotic efficacy in infections associated with significant biofilm formation.

Ort, förlag, år, upplaga, sidor
2017. Vol. 114, nr 46, s. 12184-12189
Nyckelord [en]
Amyloids, CsgA, Transthyretin, Biofilms, Curli
Nationell ämneskategori
Kemi Mikrobiologi inom det medicinska området
Identifikatorer
URN: urn:nbn:se:umu:diva-142602DOI: 10.1073/pnas.1708805114ISI: 000415173300053PubMedID: 29087319OAI: oai:DiVA.org:umu-142602DiVA, id: diva2:1162975
Tillgänglig från: 2017-12-05 Skapad: 2017-12-05 Senast uppdaterad: 2018-06-09Bibliografiskt granskad

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Ådén, JörgenAlmqvist, Fredrik

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Proceedings of the National Academy of Sciences of the United States of America
KemiMikrobiologi inom det medicinska området

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